2XPH

Crystal structure of human SENP1 with the bound cobalt

2XPH の概要

• エントリーDOI: 10.2210/pdb2xph/pdb
• 関連するPDBエントリー: 2CKG 2CKH 2G4D 2IY0 2IY1 2IYC 2IYD 2XRE
• 分子名称: SENTRIN-SPECIFIC PROTEASE 1, GLYCEROL, COBALT (II) ION, ... (4 entities in total)
• 機能のキーワード: hydrolase, cysteine protease, thiol protease
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Nucleus: Q9P0U3
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 56774.21

構造登録者

Rimsa, V.,Eadsforth, T.,Hay, R.T.,Hunter, W.N. (登録日: 2010-08-26, 公開日: 2010-09-08, 最終更新日: 2023-12-20)

主引用文献

Rimsa, V.,Eadsforth, T.,Hay, R.T.,Hunter, W.N.
The Role of Co2+ in the Crystallization of Human Senp1 and Comments on the Limitations of Automated Refinement Protocols
Acta Crystallogr.,Sect.F, 67:442-, 2011

PubMed Abstract: Metal ions often stabilize intermolecular contacts between macromolecules, thereby promoting crystallization. When interpreting a medium-resolution electron-density map of the catalytic domain of human sentrin-specific protease 1 (SENP1), a strong feature indicative of an ordered divalent cation was noted. This was assigned as Co(2+), an essential component of the crystallization mixture. The ion displays tetrahedral coordination by Glu430 and His640 from one molecule and the corresponding residues from a symmetry-related molecule. Analysis of the data derived from a previous structure of SENP1 suggested that Co(2+) had been overlooked and re-refinement supported this conclusion. High-throughput automated re-refinement protocols also failed to mark the Co(2+) position, supporting the requirement for the incorporation of as much information as possible to enhance the value of such protocols.

PubMed: 21505236
DOI: 10.1107/S1744309111005835

実験手法

X-RAY DIFFRACTION (2.4 Å)